1OHW
4-AMINOBUTYRATE-AMINOTRANSFERASE inactivated by gamma-vinyl GABA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0032144 | cellular_component | 4-aminobutyrate transaminase complex |
| A | 0032145 | molecular_function | succinate-semialdehyde dehydrogenase binding |
| A | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
| A | 0048148 | biological_process | behavioral response to cocaine |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| B | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0032144 | cellular_component | 4-aminobutyrate transaminase complex |
| B | 0032145 | molecular_function | succinate-semialdehyde dehydrogenase binding |
| B | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
| B | 0048148 | biological_process | behavioral response to cocaine |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0005829 | cellular_component | cytosol |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| C | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0032144 | cellular_component | 4-aminobutyrate transaminase complex |
| C | 0032145 | molecular_function | succinate-semialdehyde dehydrogenase binding |
| C | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
| C | 0048148 | biological_process | behavioral response to cocaine |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0005829 | cellular_component | cytosol |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| D | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0032144 | cellular_component | 4-aminobutyrate transaminase complex |
| D | 0032145 | molecular_function | succinate-semialdehyde dehydrogenase binding |
| D | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
| D | 0048148 | biological_process | behavioral response to cocaine |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES A 800 |
| Chain | Residue |
| A | ALA134 |
| A | CYS135 |
| A | CYS138 |
| B | ALA134 |
| B | CYS135 |
| B | CYS138 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES C 800 |
| Chain | Residue |
| D | ALA134 |
| D | CYS135 |
| D | CYS138 |
| C | ALA134 |
| C | CYS135 |
| C | CYS138 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP A 600 |
| Chain | Residue |
| A | CYS135 |
| A | GLY136 |
| A | SER137 |
| A | ASN140 |
| A | PHE189 |
| A | HIS190 |
| A | GLU265 |
| A | ASP298 |
| A | VAL300 |
| A | GLN301 |
| A | LYS329 |
| A | VIG700 |
| A | HOH2168 |
| A | HOH2169 |
| A | HOH2170 |
| A | HOH2171 |
| A | HOH2172 |
| B | THR353 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE VIG A 700 |
| Chain | Residue |
| A | ILE72 |
| A | PHE189 |
| A | ARG192 |
| A | GLU270 |
| A | GLN301 |
| A | LYS329 |
| A | PLP600 |
| A | HOH2172 |
| B | PHE351 |
| B | ASN352 |
| B | THR353 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP B 600 |
| Chain | Residue |
| A | THR353 |
| B | CYS135 |
| B | GLY136 |
| B | SER137 |
| B | ASN140 |
| B | PHE189 |
| B | HIS190 |
| B | GLY191 |
| B | GLU265 |
| B | ASP298 |
| B | VAL300 |
| B | GLN301 |
| B | VIG700 |
| B | HOH2047 |
| B | HOH2164 |
| B | HOH2165 |
| B | HOH2166 |
| B | HOH2167 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE VIG B 700 |
| Chain | Residue |
| A | PHE351 |
| A | ASN352 |
| A | THR353 |
| B | ILE72 |
| B | PHE189 |
| B | ARG192 |
| B | GLU270 |
| B | GLN301 |
| B | LYS329 |
| B | PLP600 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP C 600 |
| Chain | Residue |
| C | CYS135 |
| C | GLY136 |
| C | SER137 |
| C | ASN140 |
| C | PHE189 |
| C | HIS190 |
| C | GLU265 |
| C | ASP298 |
| C | VAL300 |
| C | GLN301 |
| C | VIG700 |
| C | HOH2173 |
| C | HOH2174 |
| C | HOH2175 |
| C | HOH2176 |
| C | HOH2177 |
| D | THR353 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE VIG C 700 |
| Chain | Residue |
| C | ILE72 |
| C | PHE189 |
| C | ARG192 |
| C | GLU270 |
| C | GLN301 |
| C | LYS329 |
| C | PLP600 |
| C | HOH2177 |
| D | PHE351 |
| D | ASN352 |
| D | THR353 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP D 600 |
| Chain | Residue |
| D | GLY136 |
| D | SER137 |
| D | ASN140 |
| D | PHE189 |
| D | HIS190 |
| D | GLY191 |
| D | GLU265 |
| D | ASP298 |
| D | VAL300 |
| D | GLN301 |
| D | VIG700 |
| D | HOH2196 |
| D | HOH2197 |
| D | HOH2198 |
| D | HOH2199 |
| D | HOH2200 |
| C | THR353 |
| D | CYS135 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE VIG D 700 |
| Chain | Residue |
| C | PHE351 |
| C | ASN352 |
| C | THR353 |
| D | ILE72 |
| D | PHE189 |
| D | ARG192 |
| D | GLU270 |
| D | GLN301 |
| D | LYS329 |
| D | PLP600 |
| D | HOH2200 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 40 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FLvDEVqtgGG.StGkfwahehwglddpa..DVMtfSKkmmTG |
| Chain | Residue | Details |
| A | PHE295-GLY334 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14534310 |
| Chain | Residue | Details |
| A | CYS135 | |
| A | CYS138 | |
| B | CYS135 | |
| B | CYS138 | |
| C | CYS135 | |
| C | CYS138 | |
| D | CYS135 | |
| D | CYS138 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:10393538 |
| Chain | Residue | Details |
| A | GLY136 | |
| B | GLY136 | |
| C | GLY136 | |
| D | GLY136 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14534310, ECO:0000305|PubMed:10393538 |
| Chain | Residue | Details |
| A | ARG192 | |
| B | ARG192 | |
| C | ARG192 | |
| D | ARG192 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10393538, ECO:0000269|PubMed:14534310 |
| Chain | Residue | Details |
| A | THR353 | |
| B | THR353 | |
| C | THR353 | |
| D | THR353 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P61922 |
| Chain | Residue | Details |
| A | LYS203 | |
| B | LYS203 | |
| C | LYS203 | |
| D | LYS203 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 |
| Chain | Residue | Details |
| A | LYS224 | |
| A | LYS385 | |
| B | LYS224 | |
| B | LYS385 | |
| C | LYS224 | |
| C | LYS385 | |
| D | LYS224 | |
| D | LYS385 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 16 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P61922 |
| Chain | Residue | Details |
| A | LYS251 | |
| C | LYS290 | |
| C | LYS424 | |
| C | LYS442 | |
| D | LYS251 | |
| D | LYS290 | |
| D | LYS424 | |
| D | LYS442 | |
| A | LYS290 | |
| A | LYS424 | |
| A | LYS442 | |
| B | LYS251 | |
| B | LYS290 | |
| B | LYS424 | |
| B | LYS442 | |
| C | LYS251 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10393538 |
| Chain | Residue | Details |
| A | LYS329 | |
| B | LYS329 | |
| C | LYS329 | |
| D | LYS329 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 854 |
| Chain | Residue | Details |
| A | PHE189 | steric role |
| A | ASP298 | electrostatic stabiliser |
| A | LYS329 | covalent catalysis, proton shuttle (general acid/base) |
| A | THR353 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 854 |
| Chain | Residue | Details |
| B | PHE189 | steric role |
| B | ASP298 | electrostatic stabiliser |
| B | LYS329 | covalent catalysis, proton shuttle (general acid/base) |
| B | THR353 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 854 |
| Chain | Residue | Details |
| C | PHE189 | steric role |
| C | ASP298 | electrostatic stabiliser |
| C | LYS329 | covalent catalysis, proton shuttle (general acid/base) |
| C | THR353 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 854 |
| Chain | Residue | Details |
| D | PHE189 | steric role |
| D | ASP298 | electrostatic stabiliser |
| D | LYS329 | covalent catalysis, proton shuttle (general acid/base) |
| D | THR353 | electrostatic stabiliser |
